Metabolic and stress responses of Acinetobacter oleivorans DR1 during long‐chain alkane degradation
Summary Acinetobacter oleivorans DR1 can utilize C12–C30 alkanes as a sole carbon source but not short‐chain alkanes (C6, C10). Two copies of each alkB‐, almA‐ and ladA‐type alkane hydroxylase (AH) are present in the genome of DR1 cells. Expression and mutational analyses of AHs showed that alkB1 an...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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Wiley
2017-11-01
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| Series: | Microbial Biotechnology |
| Online Access: | https://doi.org/10.1111/1751-7915.12852 |
| _version_ | 1818187945527476224 |
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| author | Chulwoo Park Bora Shin Jaejoon Jung Yunho Lee Woojun Park |
| author_facet | Chulwoo Park Bora Shin Jaejoon Jung Yunho Lee Woojun Park |
| author_sort | Chulwoo Park |
| collection | DOAJ |
| description | Summary Acinetobacter oleivorans DR1 can utilize C12–C30 alkanes as a sole carbon source but not short‐chain alkanes (C6, C10). Two copies of each alkB‐, almA‐ and ladA‐type alkane hydroxylase (AH) are present in the genome of DR1 cells. Expression and mutational analyses of AHs showed that alkB1 and alkB2 are the major AH‐encoding genes under C12–C30, and the roles of other almA‐ and ladA genes are negligible. Our data suggested that AlkB1 is responsible for long‐chain alkane utilization (C24–C26), and AlkB2 is important for medium‐chain alkane (C12–C16) metabolism. Phylogenetic analyses revealed large incongruities between phylogenies of 16S rRNA and each AH gene, which implies that A. oleivorans DR1 has acquired multiple alkane hydroxylases through horizontal gene transfer. Transcriptomic and qRT‐PCR analyses suggested that genes participating in the synthesis of siderophore, trehalose and poly 3‐hydroxybutyrate (PHB) were expressed at much higher levels when cells used C30 than when used succinate as a carbon source. The following biochemical assays supported our gene expression analyses: (i) quantification of siderophore, (ii) measurement of trehalose and (iii) observation of PHB storage. Interestingly, highly induced both ackA gene encoding an acetate kinase A and pta gene encoding a phosphotransacetylase suggested unusual ATP synthesis during C30 alkane degradation, which was demonstrated by ATP measurement using the ΔackA mutant. Impaired growth of the ΔaceA mutant indicated that the glyoxylate shunt pathway is important when C30 alkane is utilized. Our data provide insight into long‐chain alkane degradation in soil microorganisms. |
| first_indexed | 2024-12-11T23:19:06Z |
| format | Article |
| id | doaj.art-41ee24707e8c4d898a7ebb4a4be51089 |
| institution | Directory Open Access Journal |
| issn | 1751-7915 |
| language | English |
| last_indexed | 2024-12-11T23:19:06Z |
| publishDate | 2017-11-01 |
| publisher | Wiley |
| record_format | Article |
| series | Microbial Biotechnology |
| spelling | doaj.art-41ee24707e8c4d898a7ebb4a4be510892022-12-22T00:46:24ZengWileyMicrobial Biotechnology1751-79152017-11-011061809182310.1111/1751-7915.12852Metabolic and stress responses of Acinetobacter oleivorans DR1 during long‐chain alkane degradationChulwoo Park0Bora Shin1Jaejoon Jung2Yunho Lee3Woojun Park4Laboratory of Molecular Environmental Microbiology Department of Environmental Science and Ecological Engineering Korea University Seoul 02841 KoreaLaboratory of Molecular Environmental Microbiology Department of Environmental Science and Ecological Engineering Korea University Seoul 02841 KoreaNational Marine Biodiversity Institute of Korea Chungcheongnam‐Do 33662 KoreaDepartment of Life Science Chung‐Ang University Seoul 06974 KoreaLaboratory of Molecular Environmental Microbiology Department of Environmental Science and Ecological Engineering Korea University Seoul 02841 KoreaSummary Acinetobacter oleivorans DR1 can utilize C12–C30 alkanes as a sole carbon source but not short‐chain alkanes (C6, C10). Two copies of each alkB‐, almA‐ and ladA‐type alkane hydroxylase (AH) are present in the genome of DR1 cells. Expression and mutational analyses of AHs showed that alkB1 and alkB2 are the major AH‐encoding genes under C12–C30, and the roles of other almA‐ and ladA genes are negligible. Our data suggested that AlkB1 is responsible for long‐chain alkane utilization (C24–C26), and AlkB2 is important for medium‐chain alkane (C12–C16) metabolism. Phylogenetic analyses revealed large incongruities between phylogenies of 16S rRNA and each AH gene, which implies that A. oleivorans DR1 has acquired multiple alkane hydroxylases through horizontal gene transfer. Transcriptomic and qRT‐PCR analyses suggested that genes participating in the synthesis of siderophore, trehalose and poly 3‐hydroxybutyrate (PHB) were expressed at much higher levels when cells used C30 than when used succinate as a carbon source. The following biochemical assays supported our gene expression analyses: (i) quantification of siderophore, (ii) measurement of trehalose and (iii) observation of PHB storage. Interestingly, highly induced both ackA gene encoding an acetate kinase A and pta gene encoding a phosphotransacetylase suggested unusual ATP synthesis during C30 alkane degradation, which was demonstrated by ATP measurement using the ΔackA mutant. Impaired growth of the ΔaceA mutant indicated that the glyoxylate shunt pathway is important when C30 alkane is utilized. Our data provide insight into long‐chain alkane degradation in soil microorganisms.https://doi.org/10.1111/1751-7915.12852 |
| spellingShingle | Chulwoo Park Bora Shin Jaejoon Jung Yunho Lee Woojun Park Metabolic and stress responses of Acinetobacter oleivorans DR1 during long‐chain alkane degradation Microbial Biotechnology |
| title | Metabolic and stress responses of Acinetobacter oleivorans DR1 during long‐chain alkane degradation |
| title_full | Metabolic and stress responses of Acinetobacter oleivorans DR1 during long‐chain alkane degradation |
| title_fullStr | Metabolic and stress responses of Acinetobacter oleivorans DR1 during long‐chain alkane degradation |
| title_full_unstemmed | Metabolic and stress responses of Acinetobacter oleivorans DR1 during long‐chain alkane degradation |
| title_short | Metabolic and stress responses of Acinetobacter oleivorans DR1 during long‐chain alkane degradation |
| title_sort | metabolic and stress responses of acinetobacter oleivorans dr1 during long chain alkane degradation |
| url | https://doi.org/10.1111/1751-7915.12852 |
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